摘要
The Amb V allergens are small, highly disulfide-bonded ragweed pollen allergens that serve as useful models for understanding the molecular basis of the human immune response. We have produced recombinant Amb a V and Amb t V (from short and giant ragweed pollens, respectively) in Escherichia coli and have compared their structural and functional characteristics to those of the native proteins. Recombinant Amb t V was indistinguishable from native Amb t V as determined by NMR spectroscopy and antibody-binding studies. Whereas inhibition analysis showed that recombinant Amb a V possessed only ~50% of the antibody-binding activity of native Amb a V, the two proteins were similarly effective in stimulating Amb a V-specific T-cells. Our results demonstrate that even highly homologous proteins exhibit different abilities to fold into their native three-dimensional conformations and establish the potential and limits of expressing the recombinant Amb V allergens intracellularly in E. coli.
原文 | 英語 |
---|---|
頁(從 - 到) | 21119-21123 |
頁數 | 5 |
期刊 | Journal of Biological Chemistry |
卷 | 267 |
發行號 | 29 |
出版狀態 | 已發佈 - 1月 1 1992 |
對外發佈 | 是 |
ASJC Scopus subject areas
- 生物化學
- 分子生物學
- 細胞生物學